If we were to conceptualize a class of chemicals known as "TMEM58 inhibitors," these would be molecules designed to bind to and inhibit the activity of the TMEM58 protein. The development of such inhibitors would begin with a detailed understanding of the protein's structure, particularly the transmembrane regions that are accessible for potential inhibitors. Researchers would utilize structural biology tools such as X-ray crystallography, cryo-electron microscopy, and NMR spectroscopy to obtain high-resolution images of the TMEM58 protein. These images would reveal important details about the protein's topology, the orientation of its transmembrane helices, and the location of any functional domains or active sites. Such structural insights are crucial for identifying regions of the protein that are amenable to binding by small molecules or other inhibitory compounds.
Once target sites on the TMEM58 protein are identified, the design of inhibitory molecules can begin. This process often involves the use of computational chemistry to model interactions between the protein and potential inhibitors virtually, which can help in the identification and optimization of lead compounds. These candidate molecules can then be synthesized and subjected to a battery of in vitro assays to evaluate their ability to bind to and inhibit the TMEM58 protein. It is essential that these compounds exhibit selectivity, binding to TMEM58 without significantly affecting other proteins. Moreover, the chemical properties of these inhibitors-such as their solubility, stability, and ability to traverse the lipid bilayer of the cell membrane-would be of particular interest. Optimizing these properties ensures that the inhibitors can reach the TMEM58 protein at its location within the membrane and remain stable enough to exert their inhibitory effect. Through iterative cycles of testing and refinement, a collection of molecules could potentially emerge that would be categorized as "TMEM58 inhibitors," provided they demonstrate consistent and specific inhibitory activity against TMEM58.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Trichostatin A | 58880-19-6 | sc-3511 sc-3511A sc-3511B sc-3511C sc-3511D | 1 mg 5 mg 10 mg 25 mg 50 mg | $149.00 $470.00 $620.00 $1199.00 $2090.00 | 33 | |
Histone deacetylase inhibitor that can alter gene expression by changing chromatin structure. | ||||||
5-Azacytidine | 320-67-2 | sc-221003 | 500 mg | $280.00 | 4 | |
A DNA methyltransferase inhibitor that can cause hypomethylation of DNA and affect gene expression. | ||||||
Actinomycin D | 50-76-0 | sc-200906 sc-200906A sc-200906B sc-200906C sc-200906D | 5 mg 25 mg 100 mg 1 g 10 g | $73.00 $238.00 $717.00 $2522.00 $21420.00 | 53 | |
Binds to DNA and inhibits RNA polymerase, which can suppress mRNA synthesis. | ||||||
Cycloheximide | 66-81-9 | sc-3508B sc-3508 sc-3508A | 100 mg 1 g 5 g | $40.00 $82.00 $256.00 | 127 | |
Inhibits eukaryotic protein synthesis by interfering with the translocation step in protein elongation. | ||||||
Rapamycin | 53123-88-9 | sc-3504 sc-3504A sc-3504B | 1 mg 5 mg 25 mg | $62.00 $155.00 $320.00 | 233 | |
An mTOR inhibitor which can downregulate protein synthesis. | ||||||
α-Amanitin | 23109-05-9 | sc-202440 sc-202440A | 1 mg 5 mg | $260.00 $1029.00 | 26 | |
Inhibits RNA polymerase II and therefore can suppress mRNA synthesis. | ||||||
DRB | 53-85-0 | sc-200581 sc-200581A sc-200581B sc-200581C | 10 mg 50 mg 100 mg 250 mg | $42.00 $185.00 $310.00 $650.00 | 6 | |
Inhibits RNA polymerase II transcriptional elongation. | ||||||
Flavopiridol | 146426-40-6 | sc-202157 sc-202157A | 5 mg 25 mg | $78.00 $254.00 | 41 | |
Inhibits cyclin-dependent kinases and can affect transcription regulation. | ||||||
(±)-JQ1 | 1268524-69-1 | sc-472932 sc-472932A | 5 mg 25 mg | $226.00 $846.00 | 1 | |
A BET bromodomain inhibitor that can affect transcription of certain genes. | ||||||
Mithramycin A | 18378-89-7 | sc-200909 | 1 mg | $54.00 | 6 | |
Binds to DNA and prevents binding of transcription factors. | ||||||